Biochemical characterization of avirulent Agrobacterium tumefaciens chvA mutants: synthesis and excretion of beta-(1-2)glucan.

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The chvA gene product of Agrobacterium tumefaciens is required for virulence and attachment of bacteria to plant cells. Three chvA mutants were studied. In vivo, they were defective in the synthesis, accumulation, and secretion of beta-(1-2)glucan; however, the 235-kilodalton (kDa) protein known to...

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Autores principales: de Iannino, N.I., Ugalde, R.A.
Formato: JOUR
Materias:
carrier protein
glucan
membrane protein
peptide fragment
article
cell membrane
gel chromatography
genetics
metabolism
molecular weight
mutation
pathogenicity
restriction mapping
Rhizobium
Carrier Proteins
Cell Membrane
Chromatography, Gel
Glucans
Membrane Proteins
Molecular Weight
Mutation
Peptide Fragments
Restriction Mapping
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00219193_v171_n5_p2842_deIannino
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
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spelling todo:paper_00219193_v171_n5_p2842_deIannino2023-10-03T14:22:45Z Biochemical characterization of avirulent Agrobacterium tumefaciens chvA mutants: synthesis and excretion of beta-(1-2)glucan. de Iannino, N.I. Ugalde, R.A. carrier protein glucan membrane protein peptide fragment article cell membrane gel chromatography genetics metabolism molecular weight mutation pathogenicity restriction mapping Rhizobium Carrier Proteins Cell Membrane Chromatography, Gel Glucans Membrane Proteins Molecular Weight Mutation Peptide Fragments Restriction Mapping Rhizobium The chvA gene product of Agrobacterium tumefaciens is required for virulence and attachment of bacteria to plant cells. Three chvA mutants were studied. In vivo, they were defective in the synthesis, accumulation, and secretion of beta-(1-2)glucan; however, the 235-kilodalton (kDa) protein known to be involved in the synthesis of beta-(1-2)glucan (A. Zorreguieta and R. Ugalde, J. Bacteriol. 167:947-951, 1986) was present and active in vitro. was present and active in vitro. Two molecular forms of cyclic beta-(1-2)glucan, designated types I and II, were resolved by gel chromatography. Type I beta-(1-2)glucan was substituted with nonglycosidic residues, and type II beta-(1-2)glucan was nonsubstituted. Wild-type cells accumulated type I beta-(1-2)glucan, and chvA mutant cells accumulated mainly type II beta-(1-2)glucan and a small amount of type I beta-(1-2)glucan. Inner membranes of wild-type and chvA mutants formed in vitro type II nonsubstituted beta-(1-2)glucan. A 75-kDa inner membrane protein is proposed to be the chvA gene product. chvA mutant inner membranes had increased levels of 235-kDa protein; partial trypsin digestion patterns suggested that the 235-kDa protein (the gene product of the chvB region) and the gene product of the chvA region form a complex in the inner membrane that is involved in the synthesis, secretion, and modification of beta-(1-2)glucan. All of the defects assigned to the chvA mutation were restored after complementation with plasmid pCD522 containing the entire chvA region. Fil:Ugalde, R.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00219193_v171_n5_p2842_deIannino
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic carrier protein
glucan
membrane protein
peptide fragment
article
cell membrane
gel chromatography
genetics
metabolism
molecular weight
mutation
pathogenicity
restriction mapping
Rhizobium
Carrier Proteins
Cell Membrane
Chromatography, Gel
Glucans
Membrane Proteins
Molecular Weight
Mutation
Peptide Fragments
Restriction Mapping
Rhizobium
spellingShingle carrier protein
glucan
membrane protein
peptide fragment
article
cell membrane
gel chromatography
genetics
metabolism
molecular weight
mutation
pathogenicity
restriction mapping
Rhizobium
Carrier Proteins
Cell Membrane
Chromatography, Gel
Glucans
Membrane Proteins
Molecular Weight
Mutation
Peptide Fragments
Restriction Mapping
Rhizobium
de Iannino, N.I.
Ugalde, R.A.
Biochemical characterization of avirulent Agrobacterium tumefaciens chvA mutants: synthesis and excretion of beta-(1-2)glucan.
topic_facet carrier protein
glucan
membrane protein
peptide fragment
article
cell membrane
gel chromatography
genetics
metabolism
molecular weight
mutation
pathogenicity
restriction mapping
Rhizobium
Carrier Proteins
Cell Membrane
Chromatography, Gel
Glucans
Membrane Proteins
Molecular Weight
Mutation
Peptide Fragments
Restriction Mapping
Rhizobium
description The chvA gene product of Agrobacterium tumefaciens is required for virulence and attachment of bacteria to plant cells. Three chvA mutants were studied. In vivo, they were defective in the synthesis, accumulation, and secretion of beta-(1-2)glucan; however, the 235-kilodalton (kDa) protein known to be involved in the synthesis of beta-(1-2)glucan (A. Zorreguieta and R. Ugalde, J. Bacteriol. 167:947-951, 1986) was present and active in vitro. was present and active in vitro. Two molecular forms of cyclic beta-(1-2)glucan, designated types I and II, were resolved by gel chromatography. Type I beta-(1-2)glucan was substituted with nonglycosidic residues, and type II beta-(1-2)glucan was nonsubstituted. Wild-type cells accumulated type I beta-(1-2)glucan, and chvA mutant cells accumulated mainly type II beta-(1-2)glucan and a small amount of type I beta-(1-2)glucan. Inner membranes of wild-type and chvA mutants formed in vitro type II nonsubstituted beta-(1-2)glucan. A 75-kDa inner membrane protein is proposed to be the chvA gene product. chvA mutant inner membranes had increased levels of 235-kDa protein; partial trypsin digestion patterns suggested that the 235-kDa protein (the gene product of the chvB region) and the gene product of the chvA region form a complex in the inner membrane that is involved in the synthesis, secretion, and modification of beta-(1-2)glucan. All of the defects assigned to the chvA mutation were restored after complementation with plasmid pCD522 containing the entire chvA region.
format JOUR
author de Iannino, N.I.
Ugalde, R.A.
author_facet de Iannino, N.I.
Ugalde, R.A.
author_sort de Iannino, N.I.
title Biochemical characterization of avirulent Agrobacterium tumefaciens chvA mutants: synthesis and excretion of beta-(1-2)glucan.
title_short Biochemical characterization of avirulent Agrobacterium tumefaciens chvA mutants: synthesis and excretion of beta-(1-2)glucan.
title_full Biochemical characterization of avirulent Agrobacterium tumefaciens chvA mutants: synthesis and excretion of beta-(1-2)glucan.
title_fullStr Biochemical characterization of avirulent Agrobacterium tumefaciens chvA mutants: synthesis and excretion of beta-(1-2)glucan.
title_full_unstemmed Biochemical characterization of avirulent Agrobacterium tumefaciens chvA mutants: synthesis and excretion of beta-(1-2)glucan.
title_sort biochemical characterization of avirulent agrobacterium tumefaciens chva mutants: synthesis and excretion of beta-(1-2)glucan.
url http://hdl.handle.net/20.500.12110/paper_00219193_v171_n5_p2842_deIannino
work_keys_str_mv AT deianninoni biochemicalcharacterizationofavirulentagrobacteriumtumefacienschvamutantssynthesisandexcretionofbeta12glucan
AT ugaldera biochemicalcharacterizationofavirulentagrobacteriumtumefacienschvamutantssynthesisandexcretionofbeta12glucan
_version_ 1782026637353680896

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